Synthetic emmprin peptides with chitobiose substitution stimulate MMP-2 production by fibroblasts

Takehito Kawakami, Tetsuro Sameshima, Hironobu Hojo, Kaori Koga, Yoshiaki Nakahara, Bryan P. Toole, Junji Suzumiya, Yasunori Okada, Akinori Iwasaki, Kazuki Nabeshima

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)


Background: Emmprin, a glycoprotein containing two Ig domains, is enriched on tumor cell surfaces and stimulates matrix metalloproteinase (MMP) production by adjacent stromal cells. Its first Ig domain (ECI) contains the biologically active site. The dependence of emmprin activity on N-glycosylation is controversial. We investigated whether synthetic ECI with the shortest sugar is functionally active.Methods: The whole ECI peptides carrying sugar chains, a chitobiose unit or N-linked core pentasaccharide, were synthesized by the thioester method and added to fibroblasts to examine whether they stimulate MMP-2 production.Results: ECI carrying a chitobiose unit, ECI-(GlcNAc) 2, but not ECI without a chitobiose unit or the chitobiose unit alone, dose-dependently stimulated MMP-2 production by fibroblasts. ECI with longer chitobiose units, ECI-[(Man)3(GlcNAc)2], also stimulated MMP-2 production, but the extent of its stimulation was lower than that of ECI-(GlcNAc)2.Conclusions: Our results indicate that ECI can mimic emmprin activity when substituted with chitobiose, the disaccharide with which N-glycosylation starts.

Original languageEnglish
Article number300
JournalBMC cancer
Publication statusPublished - 2011 Jul 17
Externally publishedYes

ASJC Scopus subject areas

  • Oncology
  • Genetics
  • Cancer Research


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